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In this issue |
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Mutations in the protein huntingtin that expand its N-terminal
polyglutamine tract cause the inherited neurodegenerative disorder Huntington
disease. The expanded polyglutamine repeat is thought to reduce the solubility
of the protein, resulting in formation of the characteristic
nuclear/perinuclear aggregates that probably cause neuronal cell death.
Phillippe Djian and co-workers now show that huntingtin binds to microtubules.
They demonstrate that the protein interacts specifically with ß-tubulin
(but not 
-tubulin or MAP2) in lymphoblasts and brain. In addition, they
demonstrate that it copurifies with polymerized microtubules in vitro and
colocalizes with microtubules and centrosomes in vivo. This ability to
associate with ß-tubulin seems to be a property of both wild-type and
mutant huntintin. The authors suggest that a high density of microtubules in
the perinuclear region could make huntingtin aggregates more likely to develop
in the perinuclear region. Since ß-tubulin is more abundant in neurons
than in any other cell type, such inclusions might form more rapidly in these
cells.
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